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TitleFunctional link between DEAH/RHA helicase Prp43 activation and ATP base binding.
Journal, issue, pagesNucleic Acids Res., Vol. 45, Page 1539-1552, Year 2017
Publish dateMay 4, 2016 (structure data deposition date)
AuthorsRobert-Paganin, J. / Halladjian, M. / Blaud, M. / Lebaron, S. / Delbos, L. / Chardon, F. / Capeyrou, R. / Humbert, O. / Henry, Y. / Henras, A.K. ...Robert-Paganin, J. / Halladjian, M. / Blaud, M. / Lebaron, S. / Delbos, L. / Chardon, F. / Capeyrou, R. / Humbert, O. / Henry, Y. / Henras, A.K. / Rety, S. / Leulliot, N.
External linksNucleic Acids Res. / PubMed:28180308
MethodsX-ray diffraction
Resolution2.935 Å
Structure data

PDB-5jpt:
CRYSTAL STRUCTURE OF THE PRP43P DEAH-BOX RNA HELICASE IN COMPLEX WITH CDP
Method: X-RAY DIFFRACTION / Resolution: 2.935 Å

Chemicals

ChemComp-CDP:
CYTIDINE-5'-DIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-ACT:
ACETATE ION

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsHYDROLASE / RNA helicase / Prp43p / DEAH/RHA

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